Modified protein adhesives and lignocellulosic composites made from the adhesives

ABSTRACT

An adhesive composition made by reacting a soy protein with at least one compound under conditions sufficient for introducing additional phenolic hydroxyl functional groups, amine functional groups, and/or thiol functional groups into the soy protein structure.

PRIORITY

This application claims priority to U.S. Provisional Application60/380,366, filed May 13, 2002, and incorporated herein by reference.

FIELD

The present disclosure relates to adhesives and lignocellulosiccomposites made from the adhesives.

BACKGROUND

Lignocellulosic-based composites are formed from small dimension piecesof cellulosic material that are bonded with an adhesive (i.e., abinder). In general, solid wood is fragmented into smaller pieces suchas strands, fibers, and chips. An adhesive composition then is added tothe wood component. The resulting mixture is subjected to heat andpressure resulting in a composite. The adhesive mix typically is theonly non-lignocellulosic component.

The most commonly used wood adhesives are phenol-formaldehyde resins(PF) and urea-formaldehyde resins (UF). There are at least two concernswith PF and UF resins. First, volatile organic compounds (VOC) aregenerated during the manufacture and use of lignocellulosic-basedcomposites. An increasing concern about the effect of emissive VOC,especially formaldehyde, on human health has prompted a need for moreenvironmentally acceptable adhesives. Second, PF and UF resins are madefrom petroleum-derived products. The reserves of petroleum are naturallylimited. The wood composite industry would greatly benefit from thedevelopment of formaldehyde-free adhesives made from renewable naturalresources.

Soy protein was used as a wood adhesive for the production of plywoodfrom the 1930's to the 1960's. Petroleum-derived adhesives replaced soyprotein adhesives due to the relatively low bonding strength and waterresistance of soy protein adhesives. However, soy protein is aninexpensive, abundant, renewable material that is environmentallyacceptable.

SUMMARY OF THE DISCLOSURE

Disclosed herein are adhesive compositions made by reacting a proteinwith at least one compound under conditions sufficient for introducingadditional phenolic functional groups, amine functional groups, and/orthiol functional groups into the protein structure.

One example of an adhesive composition disclosed herein includes areaction product of soy protein with at least one compound underconditions sufficient for introducing additional phenolic hydroxyl,amino, imino and/or thiol functional groups into the soy proteinstructure. The additional functional groups typically are present interminal, pendant, or terminal and pendant positions in the soy proteinstructure.

A further example of an adhesive composition disclosed herein includes areaction product of soy protein and at least one compound, wherein thecompound includes (i) at least one first functional group selected fromphenolic hydroxyl, thiol, amino, and imino, and (ii) at least one secondfunctional group for covalently bonding the compound to the soy protein.

In a first, more specific approach, the adhesive composition includes areaction product of protein and a compound, wherein the compoundincludes (i) at least one first functional group selected from phenolichydroxyl and thiol and (ii) at least one amino functional group, and theamino functional group of the compound covalently bonds to a carboxylicacid functional group of the protein.

In a second, more specific approach, the adhesive composition includesmodified protein made by initially reacting protein and a first compoundthat includes at least one nitrogen-containing functional group underconditions sufficient for covalently bonding the nitrogen-containingfunctional group with a functional group of the protein resulting in anamine-augmented protein. The amine-augmented protein then is reactedwith at least one phenolic compound under conditions sufficient forcovalently bonding the phenolic compound to the amine-augmented proteinto produce the modified protein adhesive.

In a third, more specific approach, the adhesive composition includes amodified protein made by initially reacting protein and a phenolic orthiol compound under conditions sufficient for forming at least oneether, ester or amide linkage between the phenolic or thiol compound andthe protein resulting in a thiol- or phenolic hydroxyl-augmentedprotein. The thiol- or phenolic hydroxyl-augmented protein then isreacted with a compound that includes at least one nitrogen-containingfunctional group under conditions sufficient for covalently bonding atleast one amino functional group to the thiol- or phenolichydroxyl-augmented protein.

Also disclosed herein are methods for making lignocellulosic compositesfrom the adhesive compositions and the resulting composites.

BRIEF DESCRIPTION OF THE DRAWINGS

Certain embodiments will be described in more detail with reference tothe following drawing:

FIG. 1 shows a synthesis scheme for producing an example of thepresently described adhesive;

FIG. 2 is a graph depicting the lap-shear strength of examples of thepresently described adhesives and a comparative example;

FIG. 3 is a graph depicting the lap-shear strength of an example of thepresently described adhesives and a comparative example;

FIG. 4 shows a synthesis scheme for producing a further example of thepresently described adhesive; and

FIG. 5 is a graph depicting the lap-shear strength of an adhesive madeaccording to the synthesis scheme shown in FIG. 4.

DETAILED DESCRIPTION OF SEVERAL EMBODIMENTS

The presently disclosed adhesives may be made by modifying a protein toincrease the number of phenolic hydroxyl groups, amino or imino, and/orthiol (i.e., mercapto) functional groups existing in the proteinstructure. In other words, the resulting modified protein structure(i.e., the protein residue) includes an additional number of covalentlybonded phenolic hydroxyl groups, amino or imino, and/or thiol functionalgroups beyond those already existing in the unmodified proteinstructure. In particular, the additional phenolic hydroxyl groups, aminoor imino, and/or thiol groups are introduced in terminal and/or pendantpositions in the protein residue structure. As a result of theirterminal and/or pendant position, the additional phenolic hydroxylgroups, amino, imino, or thiol groups are free for substrate adhesivebonding and crosslinking when the adhesive composition is heated asdescribed below. These additional free functional groups typically arecovalently bonded to the protein structure via linking groups such asamides, ethers, or esters.

The modified protein structure may include one or more types ofadditional free functional groups. For example, the modified proteinstructure may include only phenolic hydroxyl, amino or thiol groups.However, according to another embodiment, the modified protein structuremay include additional phenolic hydroxyl groups and amino groups. In anadditional variant, the modified protein structure may includeadditional thiol groups and phenolic hydroxyl groups. In a furthervariant, the modified protein structure may include additional phenolichydroxyl groups, thiol groups, and amino groups.

According to particular examples of the adhesive, the protein may bemodified to incorporate about 0.1 weight percent to about 30 weightpercent additional phenolic compounds, about 0.1 weight percent to about30 weight percent additional amine compounds, and/or about 0.1 weightpercent to about 30 weight percent thiol compounds, based on the totalweight of the modified protein. The inventors have found that augmentingthe number of amine, phenolic groups, and/or thiol groups in a proteinstructure provides an adhesive having superior adhesive strength andwater resistance.

The protein undergoing modification typically is any protein that isreadily available from a renewable source. Examples of such proteinsinclude soy protein, keratin, gelatin, collagen, gluten, and casein. Theprotein may have been pretreated to obtain a material that is soluble ordispersible in water as is known in the art.

Soy protein is an exemplary protein for use in the presently describedadhesives. Soybeans contain about 38 weight percent protein with theremaining portion comprising carbohydrates, oils and moisture. Soybeansare processed to increase the amount of soy protein in the processedproduct. Soy protein products of any form may be utilized in thedisclosed adhesive compositions. The three most common soy proteinproducts are soy flour, soy protein concentrate, and soy protein isolate(SPI). One difference between these products is the amount of soyprotein. Soy flour includes approximately 50 weight percent protein, soyprotein concentrate includes at least about 65 weight percent protein(dry weight), and SPI includes at least about 85 weight percent protein(dry weight). According to certain embodiments of the adhesivecomposition, the soy protein is SPI.

The protein may be prepared for use in the adhesive compositions in anymanner. Typically, the protein is included in a carrier or deliveryliquid such as water or similar solvent. In particular, the protein maybe dissolved in water and the resulting aqueous solution mixed with themodifying reactant(s) described above. The aqueous adhesive solution maybe prepared, for example, by initially mixing the protein in water andadjusting the pH of the mixture to the desired range. When the proteinis mixed with the modifying reactant(s), the pH of the protein part maybe acidic or alkaline. For example, the pH of the protein part may beabout 5 to about 8 for the reaction of the protein with an aminecompound. However, when the modified protein is used as a wood adhesive,the pH value should be between about 4.5 to about 11. The pH may beadjusted by adding basic substances such as, for example, alkalihydroxides, or by adding acidic substances such as inorganic acids ororganic acids. The amount of protein dissolved in the water may beadjusted to provide the desired solids content for the adhesivecomposition. The protein solids content may be, for example, from about10 to about 60 weight percent. The protein solution may be freeze-driedat this stage of formulation or it may remain as a liquid solution. Ifthe protein solution is freeze-dried, water (or the appropriate carrierfluid) is simply added to the freeze-dried substance prior to use.Freeze-drying will reduce the cost of transporting the adhesive.

There are a number of synthesis variations for modifying the protein toincrease the number of phenolic hydroxyl groups, amino or iminofunctional groups, and/or thiol functional groups. In a first variant,the protein may be reacted with a multifunctional compound that includes(i) a first functional group selected from a phenolic hydroxyl, a thiol,or an amino and (ii) a second functional group that can form a covalentbond with the protein. The second functional group may be an amino,carboxyl, hydroxyl, or similar protein-reactive group. In examples ofthe first variant, the protein may be reacted with a multifunctionalcompound that includes both phenolic hydroxyl and amino functionalgroups (or both thiol and amino functional groups) that can beintroduced into the protein structure. The amino functional groups reactwith the carboxyl functional groups of the protein to form amide linkinggroups. In a second variant, the protein may be initially reacted with anitrogen-donating compound for producing an amine-augmented protein thatis subsequently reacted with a phenolic hydroxyl-donating compound forproducing the final modified protein adhesive. In a third variant, theprotein may be initially reacted with a phenolic hydroxyl-donatingcompound for producing a phenolic hydroxyl-augmented protein that issubsequently reacted with a thiol- or nitrogen-donating compound forproducing the final modified protein adhesive. Each synthesis variantwill be described below in more detail. In all of the variants, all ofthe reactants may be in the form of aqueous solutions or dispersions.Thus, volatile organic solvents as carrier fluids can be avoided.

With reference to the first variant, illustrative multifunctionalcompounds for reacting with the protein to introduce free phenolichydroxyl groups include dopamine (i.e., 3,4-dihydroxyphenylethylaminehydrochloride), tyramine (4-hydroxyphenylethylamine hydrochloride), DOPA(3,4-dihydroxyphenyl-L-alanine), 2-aminophenol, 3-aminophenol, and4-aminophenol. Illustrative multifunctional compounds for reacting withthe protein to introduce free thiol groups include cysteamine, cysteine,glutathione, five-membered dithiocarbonates (i.e., compounds with thebasic structure of 1,3-oxathiolane-2-thione), γ-thiobutyrolactone,mercaptoacetic acid, 2-mercaptoethanol, 3-mercaptopropionic acid, and(3-mercaptopropyl)trimethoxysilane. Illustrative multifunctionalcompounds for reacting with the protein to introduce free amino groupsinclude alkyl amines (e.g., 1,3-diaminopropane, 1,6-hexanediamine,ethylene diamine, diethylenetriamine), unsaturated hydrocarbon amines(e.g., allylamine), hydroxy amines (e.g.,ethanolamine, hydroxyamine),amidines (e.g., melamine), imines (e.g., polyethyleneimine), amino acids(e.g., 4-aminobutyric acid, 6-aminocaprioc acid), polyamines,polyamides, and mixtures thereof. In the case of the diamines, triaminesor polyamines, one or more, but not all, of the amino groups may formthe covalent bond with the protein. The amino group(s) that do notcovalently bond with the protein then are available to serve as the freefunctional group for adhesive bonding purposes.

The multifunctional compounds may be reacted with the protein via achemical process that includes blocking certain phenolic hydroxylgroups, thiol groups and/or amino groups of the multifunctionalcompounds. Alternatively, the multifunctional compounds may be reactedwith a protein in a one-step enzymatic process that does not requireblocking of phenolic hydroxyl groups, thiol groups and/or amino groupsof the multifunctional compounds.

With respect to the chemical process, the phenolic hydroxyl groups,thiol groups and/or amino groups whose reaction with the protein duringthe protein modification is undesirable would be initially protectedwith a group that is non-reactive with functional groups of the protein.Such protection processes may include the formation of ethers, esters,amides, or thiol-esters. The protein then is reacted with theselectively protected multifunctional compound under conditionssufficient for forming a covalent bond between a functional group of theprotein (typically a carboxylic acid, amino, hydroxyl or thio functionalgroup) and an amino group or carboxylic acid group of themultifunctional compound. The conditions for this reaction may varydepending upon the protein and multifunctional compound but, in general,the reaction may occur at about 4 to about 200° C. In addition, theremay be additives or catalysts involved in this reaction such ascarboxylic-acid-activating agents (e.g.,1-(3-dimethylaminopropyl)-3-ethylcarbodiimide hydrochloride (EDC),transglutaminase, and lipase). Finally, the remaining protected phenolichydroxyl groups, thiol groups and/or amino groups of the modifiedprotein are deprotected by reaction with acids such as HBr, acetic acid,trifluoracetic acid, sulfuric acid, and HCl or with an alkali such assodium hydroxide. The conditions for the unblocking reaction may varydepending upon the protein and unblocking reactant but, in general, thereaction may occur at about 20 to about 150° C.

With respect to the enzymatic process, the multifunctional compound, theprotein and an enzyme catalyst may be mixed together. The enzymecatalyzes the formation of an amide or an ester covalent bond between acarboxylic acid group of the protein and an amino group/hydroxyl groupof the multifunctional compound or between an amino group/hydroxyl groupof the protein and a carboxylic acid of the multifunctional compound.Illustrative enzyme catalysts include transglutaminases and lipases. Theconditions for the catalyzed enzymatic reaction may vary depending uponthe protein, enzyme, and multifunctional compound but, in general, thereaction may occur at about 4 to about 70° C. The pH value should be atabout 3 to about 9.

The second variant involves reacting the protein with anitrogen-donating compound under conditions sufficient for covalentlybonding at least one amino group to the protein structure. According toillustrative examples, the nitrogen-donating compound reacts with thecarboxylic acid groups of the protein. The reaction conditions may varydepending upon the particular protein and nitrogen-donating compound,but in general the reaction temperature may range from about 4 to about200° C. Additives or catalysts that may be involved in this reactioninclude carboxylic-acid-activating agents such as1-(3-dimethylaminopropyl)-3-ethylcarbodiimide hydrochloride (EDC),transglutaminase, and lipase.

Suitable nitrogen-donating compounds include compounds that contain atleast one amino or imino group. Illustrative nitrogen-donating compoundsinclude alkyl amines (e.g., 1,3-diaminopropane, 1,6-hexanediamine,ethylene diamine, diethylenetriamine), unsaturated hydrocarbon amines(e.g., allylamine), hydroxy amines (e.g.,ethanolamine, hydroxyamine),amidines (e.g., melamine), imines (e.g., polyethyleneimine), amino acids(e.g., 4-aminobutyric acid, 6-aminocaprioc acid), polyamines,polyamides, and mixtures thereof. The nitrogen-donating compound may bewater-soluble or water-dispersible.

The phenolic hydroxyl-donating compound may react with theamine-augmented protein by various synthetic approaches. For example,via oxidation intermediates (e.g., quinones and aromatic rings) ofphenolic hydroxyl groups of the phenolic-donating compound reacting withamino functional group of the amine-augmented protein. Illustrativephenolic-donating compounds include dopamine, DOPA(3,4-dihydroxyphenylalanine); caffeic acid; catechol; 4-methylcatechol;4-hydroxycinnamic acid; 4-hydroxy-3-methoxycinnamic acid;4-hydroxy-3,5-dimethoxycinnamic acid; tannin; flavonoids; lignin; andpoly(4-vinylphenol). The conditions for the reaction may vary dependingupon the protein and phenolic hydroxyl-donating compound but, ingeneral, the reaction may occur during the pressing of wood compositesat about 100 to about 200° C. for about 0.5 to about 10 minutes. Theamine-augmented protein can also be used as one part of a two-partadhesive system in which the second part is the phenolichydroxyl-donating compound.

With respect to the third variant, the protein is initially reacted witha phenolic hydroxyl-donating compound under the conditions describedabove. The phenolic hydroxyl-augmented protein then is reacted with athiol-donating or nitrogen-donating compound under the conditionsdescribed above. Illustrative thiol-donating compounds includecysteamine, cysteine, glutathione, five-membered dithiocarbonates (i.e.,compounds with the basic structure of 1,3-oxathiolane-2-thione),γ-thiobutyrolactone, mercaptoacetic acid, 2-mercaptoethanol,3-mercaptopropionic acid, and (3-mercaptopropyl)trimethoxysilane. Thephenolic hydroxyl-augmented protein can also be used as one part of atwo-part adhesive system in which the second part is thenitrogen-donating compound or thiol-donating compound.

According to particular embodiments, the phenolic compound that iscovalently bonded to the protein includes two phenolic hydroxyl groupsin an ortho position relative to each other on the aromatic ring. Twophenolic hydroxyl groups should provide superior bonding strength. Ifonly one phenolic hydroxyl group is present, an enzyme such asphenol-oxidative enzymes such as laccases, polyphenoloxidases ortyrosinases may be added as a curing agent.

The adhesive composition may also include additives and fillers found inlignocellulosic adhesives such as bactericides, insecticides, silica,wheat flour, tree bark flour, nut shell flour and the like.

The adhesive compositions are heat-curable. Such curing typically occursduring the hot pressing step of the lignocellulosic composite formation.Thus, the cure temperature of the adhesive composition is tailored sothat it coincides with the heating temperatures used in compositeformation. Such cure temperatures may range, for example, from about 100to about 200° C., more particularly from about 120 to about 170° C.

Lignocellulosic composites that can be produced with the adhesivesdescribed herein include particleboard, oriented strand board (OSB),waferboard, fiberboard (including medium-density and high-densityfiberboard), parallel strand lumber (PSL), laminated strand lumber(LSL), and similar products. In general, these composites are made byfirst blending comminuted lignocellulosic materials with an adhesivethat serves as a binder that adheres the comminuted lignocellulosicmaterials into a unitary densified mass. Examples of suitablelignocellulosic materials include wood, straw (including rice, wheat andbarley), flax, hemp and bagasse. The comminuted lignocellulosicmaterials can be in any processed form such as chips, flakes, fibers,strands, wafers, trim, shavings, sawdust, straw, stalks and shives. Theresultant mixture is formed into the desired configuration such as amat, and then processed, usually under pressure and with heat, into thefinal product. Processes are generally carried out at temperatures offrom about 120 to 225° C. in the presence of varying amounts of steam,generated by liberation of entrained moisture from the lignocellulosematerials. Thus, the moisture content of the lignocellulose material maybe between about 2 and about 20 percent by weight, before it is blendedwith the adhesive.

The amount of adhesive mixed with the lignocellulosic particles may varydepending, for example, upon the desired composite type, lignocellulosicmaterial type and amount of, and particular type of, adhesivecomposition. In general, about 1 to about 12, more particularly about 3to about 10, weight percent adhesive may be mixed with thelignocellulosic material, based on the total combined weight of adhesiveand lignocellulosic material. The mixed adhesive composition may beadded to the comminuted lignocellulosic particles by spraying or similartechniques while the lignocellulosic particles are tumbled or agitatedin a blender or similar mixer. For example, a stream of the comminutedlignocellulosic particles may be intermixed with a stream of the mixedadhesive composition and then be subjected to mechanical agitation.

The adhesive compositions also may be used to produce plywood, hardboardor laminated veneer lumber (LVL). The adhesive composition may beapplied onto veneer surfaces by roll coating, knife coating, curtaincoating, or spraying. A plurality of veneers are then laid-up to formsheets of required thickness. The mats or sheets are then placed in aheated press (e.g., a platen) and compressed to effect consolidation andcuring of the materials into a board. Fiberboard may be made by the wetfelted/wet pressed method, the dry felted/dry pressed method, or the wetfelted/dry pressed method.

The presently disclosed adhesive provides a strong bond between thelignocellulosic particles or fractions. The adhesive also providesstructural composites with high mechanical strength. In addition, theadhesive composition is substantially free of formaldehyde (includingany compounds that may degenerate to form formaldehyde). For example,the adhesive compositions do not contain any formaldehyde (andformaldehyde-generating compounds) that is detectable by conventionalmethods or, alternatively, the amount of formaldehyde (andformaldehyde-generating compounds) is negligible from an environmentaland workplace regulatory standpoint.

The specific examples described below are for illustrative purposes andshould not be considered as limiting the scope of the appended claims.

EXAMPLE 1 Preparation of Alkali-Modified Soy Protein Isolate

SPI powder (10 g) was mixed with 140 ml of distilled water at roomtemperature and then stirred for 120 minutes. The pH value of themixture was then adjusted to 10 using sodium hydroxide (1 M). Themixture was subsequently mixed in a shaker at 50° C. and 180 rpm for 120minutes. The insoluble portion was removed through filtration and theaqueous SPI solution was freeze-dried.

EXAMPLE 2 Preparation of Phenolic Hydroxyl-Augmented SPI-Dopamine

A reaction synthesis for preparing a phenolic hydroxyl-augmentedSPI-dopamine is shown in FIG. 1. A mixture of dopamine (DA) (1.0 g) anddichlorodiphenyl methane (3.16 g) was slowly stirred at 1 90° C. Afterthe reaction started, as evidenced by rigorous gas evolution, thereaction mixture was stirred rapidly at 190° C. for 6 minutes. Themixture was cooled to room temperature and then washed by diethyl ether.The product ((1)—O, O′-diphenylmethyl-dopamine hydrochloride) wascrystallized from methanol and ethyl acetate (1.36 g, 73 percent).

To a suspension of the alkaline SPI of Example 1 (1.0 g) in 40 ml oftetrahydrofuran (THF)-H₂O (1:1, v/v) was added a solution of compound 1(2.07 g) in THF-H₂O (1:1, v/v) (20 ml). The resulting mixture wasadjusted to a pH value of 5.5. A solution of1-(3-dimethylaminopropyl)-3-ethylcarbodiimide hydrochloride (EDC) (1.8g) and THF-H2O (1:1, v/v) (20 ml) was added to the reaction mixturedropwise in 1 hour while maintaining the pH value at 5.5. The reactionmixture was stirred overnight and then centrifuged. The precipitate 2was collected and washed with EtOAc (2 times) and deionized water (2times).

To a solution of the protected SPI-DA (compound 2) (1.0 g) in TFA (10ml) was added 33 percent HBr-AcOH (10 ml) with stirring. The mixture wasstirred for 1 hour at room temperature. The deprotected SPI-DA (compound3) was precipitated by addition of diethyl ether, washed extensivelywith water-ethanol (1:4, v/v), and then freeze-dried.

The amount of dopamine in the dopamine-modified SPI was determined asexplained below. The protected SPI-DA (20 mg) was hydrolyzed in 4 ml of6N HCl solution for 24 hours at 110° C. The hydrolyzed product wasdiluted with deionized water to 100 ml. To 1.0 ml of the dilutedsolution was added water (1.0 ml), sodium nitrite-sodium molybdate stocksolution (NaNO₂, 100 g and Na₂MoO₄, 100 g in 1.0 liter of deionizedwater) (1.0 ml), and 1N sodium hydroxide (1.0 ml). Absorbance of theresulting solution was measured at 500 nm, and corrected by a control(Protected SPI-DA was replaced with the alkaline SPI in the aboveprocedure). The concentration of dopamine was then determined by use ofa dopamine standard curve. The dopamine standard curve was obtained asfollows: an aqueous dopamine solution (1.0 ml) with predeterminedconcentration of dopamine was mixed with water (1.0 ml), the sodiumnitrite-sodium molybdate stock solution (1.0 ml), and 1N sodiumhydroxide (1.0 ml). Absorbance of the resulting solution was read at 500nm. The linear relationship between the absorbance and the concentrationof dopamine was used to construct a dopamine standard curve.

EXAMPLE 3 Preparation and Testing Wood Composites

A solution of water and the modified SPI of Example 2 (6:1 wt. ratio)was applied to one surface of a maple veneer strip (100×60 mm, 0.6 mmthick). About 2.5 mg modified SPI was applied to the maple veneer. Thebonding area was 2×2.5 cm. Two pieces of maple veneer strips werestacked together and hot-pressed at 120° C. for 10 minutes. The appliedpressure was 20 kg/cm².

Lap-shear strengths of the resulting wood assembly specimens were testedusing an Instron TTBML testing machine with a crosshead speed of 1.0mm/minute. The maximum shear strength at breakage was recorded. In waterresistance testing, the specimens were soaked in water at roomtemperature for 24 hours then dried at room temperature in a fume hoodfor 24 hours and the shear strengths of the specimens were measured. Thesoaking-and-drying cycle was repeated and the shear strengths weremeasured after each soaking-and-drying cycle.

The lap-shear strength results are shown in FIGS. 2 and 3. The amount ofdopamine grafted to the SPI was varied by changing the amount ofcompound 1 and EDC. As shown in FIG. 2 grafting of the dopamine (DA) tothe SPI greatly increased the shear strength compared to an ungraftedalkali-SPI. Even after three soaking-and-drying cycles, the shearstrengths of the wood specimens bonded with SPI-DA did not decrease. Asa matter of fact, the shear strengths of specimens bonded with SPI-DAwith a DA content of 14.73 weight percent increased after the firstsoaking-and-drying cycle. When the DA content increased from 4.12 weightpercent to 8.95 weight percent, the shear strengths increasedsignificantly. However, the shear strengths decreased when the DAcontent increased from 8.95 weight percent to 14.73 weight percent. Theincrease in the shear strengths was due to the phenolic hydroxy groupsin DA. FIG. 3 demonstrates the difference in shear strength betweenprotected SPI-DA (referred to as compound 2 in FIG. 1) and the unblockedSPI-DA (referred to as compound 3 in FIG. 1).

EXAMPLE 4 Synthesis of S-Acetyl Cysteamine

The thiol groups of cysteamine were blocked according to the followingprocedure. Acetyl chloride (10 mL) was added dropwise to a solution ofcysteamine hydrochloride (2 g) and trifluoroacetic acid (10 ml). Thereaction mixture was stirred under room temperature for 1 hour. Theproduct precipitated out by adding ethyl ether. The precipitate wascrystallized in methanol-ethyl ether to give pure S-acetyl cysteamine(“ACA”).

EXAMPLE 5 Preparation of Thiol-Augmented SPI

A reaction synthesis for preparing a thiol-augmented SPI is shown inFIG. 4. A solution of ACA (3.36 g, 21.47 mmol) and THF/H₂O (1:1, v/v;100 mL) was added to a suspension of the alkaline SPI of Example 1 (5.00g) in 200 ml of THF/H₂O (1:1, V/V). The pH value of the resultingmixture was adjusted to 5.5. A solution of EDC (9 g, 46.9 mmol) andTHF/H₂O (1:1, V/V; 100 ml) was added dropwise to the reaction mixture in1 hour while maintaining the pH value at 5.5. The reaction mixture wasstirred overnight and then centrifuged. The precipitate was collectedand washed with ethyl acetate (2 times) and deionized water (2 times)and then freeze-dried. Several different modified SPI-ACAs were producedunder the reaction conditions shown below in Table 1.

TABLE 1 Modified SPIs SPI ACA EDC A1 5 g 0.84 g (5.37 mmol) 2.25 g(11.74 mmol) A2 5 g 1.68 g (10.73 mmol) 4.50 g (23.47 mmol) A3 5 g 3.36g (21.46 mmol) 9.00 g (46.95 mmol)

In order to de-protect the thiol groups, a 0.2 N NaOH solution (100 mL)was bubbled with a nitrogen stream for 15 min. SPI-ACA (2.0 g) was addedin the NaOH solution and stirred for 1 hour. The resulting mixture wasneutralized by HCl to pH 7 and ultrafiltrated with a membrane (10,000kDa molecular weight cutoff) under an atmosphere of nitrogen. The SPI-CAwas freeze-dried.

EXAMPLE 6 Preparation and Testing Wood Composites

Maple veneer with a thickness of 0.6 mm was cut into pieces with thedimension of 7.5×12 cm. A glue mixture containing water/SPI-CA (6:1weight ratio) was pasted to one side of the maple veneer samples. Theadhesive-pasted area for each piece of veneer sample was 1.5×12 cm. Theamount of glue was 2.5 mg/cm² (dry weight). Two pieces ofadhesive-pasted veneer were lapped together and then pressed at 20kg/cm² and 120° C. for 10 minutes. Subsequently, the plywood sample wascut into 6 specimens. Each specimen had a bond area of 2×1.5 cm².Lap-shear strengths of the resulting wood assembly specimens were testedas described above in Example 3. The results are shown in FIG. 5.

Having illustrated and described the principles of the disclosedcompositions, methods and composites with reference to severalembodiments, it should be apparent that these compositions, methods andcomposites may be modified in arrangement and detail without departingfrom such principles.

1. An adhesive composition comprising a reaction product of soy proteinand a compound, wherein the compound includes (i) at least one firstfunctional group selected from phenolic hydroxyl or thiol and (ii) atleast one amino functional group, and the amino functional group of thecompound covalently bonds to a carboxylic acid functional group of thesoy protein.
 2. An adhesive composition according to claim 1, whereinthe phenolic hydroxyl functional group includes two phenolic hydroxylgroups in an ortho position relative to each other on the aromatic ring.3. An adhesive composition comprising a modified soy protein made by:(i) reacting a soy protein and a first compound that contains at leastone amino functional group under conditions sufficient for covalentlybonding the amino functional group with a functional group of the soyprotein resulting in an amine-augmented soy protein; and (ii) reactingthe amine-augmented soy protein with at least one phenolic compoundunder conditions sufficient for covalently bonding the phenolic compoundto the amine-augmented soy protein resulting in aphenolic/amine-augmented soy protein.
 4. An adhesive compositionaccording to claim 3, wherein the phenolic compound includes twophenolic hydroxyl groups in an ortho position relative to each other onthe aromatic ring.
 5. An adhesive composition comprising a modified soyprotein made by: (i) reacting a soy protein and a phenolic compoundunder conditions sufficient for forming at least one ether, ester oramide linkage between the phenolic compound and the soy proteinresulting in a phenolic hydroxyl-augmented soy protein; and (ii)reacting the phenolic hydroxyl-augmented soy protein with a compoundthat includes at least one thiol or amino functional group underconditions sufficient for covalently bonding the thiol or aminofunctional group to the phenolic hydroxyl-augmented soy proteinresulting in a phenolic hydroxyl/thiol-augmented soy protein or aphenolic hydroxyl/amino-augmented soy protein.
 6. An adhesivecomposition according to claim 5, wherein the phenolic compound includestwo phenolic hydroxyl groups in an ortho position relative to each otheron the aromatic ring.
 7. An adhesive composition comprising the reactionproduct of soy protein with at least one compound under conditionssufficient for introducing additional functional groups into the soyprotein structure, wherein the additional functional groups comprise atleast one group selected from phenolic hydroxyl, amino, imino or thiol,and the additional functional groups are present in terminal, pendant,or terminal and pendant positions in the soy protein structure.
 8. Amethod for making a lignocellulosic composite, comprising: applying theadhesive composition of claim 1 to at least one lignocellulosicsubstrate; and bonding the adhesive-applied lignocellulosic substrate toat least one other lignocellulosic substrate.
 9. A method for making alignocellulosic composite, comprising: applying the adhesive compositionof claim 3 to at least one lignocellulosic substrate; and bonding theadhesive-applied lignocellulosic substrate to at least one otherlignocellulosic substrate.
 10. A method for making a lignocellulosiccomposite, comprising: applying the adhesive composition of claim 5 toat least one lignocellulosic substrate; and bonding the adhesive-appliedlignocellulosic substrate to at least one other lignocellulosicsubstrate.
 11. An adhesive composition according to claim 1, wherein thefirst functional group comprises a phenolic hydroxyl group, and theamino functional group of the compound covalently bonded to thecarboxylic acid functional group of the soy protein forms an amidelinking group.
 12. An adhesive composition according to claim 1, whereinthe first functional group comprises a thiol group, and the aminofunctional group of the compound covalently bonded to the carboxylicacid functional group of the soy protein forms an amide linking group.13. An adhesive composition according to claim 11, wherein the compoundis selected from dopamine, tyramine, DOPA, 2-aminophenol, 3-aminophenol,or 4-aminophenol.
 14. An adhesive composition according to claim 12,wherein the compound is selected from cysteamine, cysteine, orglutathione.
 15. An adhesive composition according to claim 1,comprising an aqueous solution of the reaction product.
 16. An adhesivecomposition according to claim 7, comprising an aqueous solution of thereaction product.
 17. An adhesive composition according to claim 1,wherein the first functional group is initially blocked with aprotective group, the resulting protected compound is reacted with thesoy protein, and then the protective group is removed from the resultingmodified soy protein to produce the reaction product.
 18. A method formaking a lignocellulosic composite, comprising: applying the adhesivecomposition of claim 7 to at least one lignocellulosic substrate; andbonding the adhesive-applied lignocellulosic substrate to at least oneother lignocellulosic substrate.
 19. An adhesive composition comprisinga reaction product of soy protein and at least one compound, wherein thecompound includes (i) at least one first functional group selected fromphenolic hydroxyl, thiol, amino, or imino, and (ii) at least one secondfunctional group for covalently bonding the compound to the soy protein.20. An adhesive composition according to claim 19, wherein the secondfunctional group comprises at least one group selected from hydroxyl,carboxyl, or amino.
 21. A method for making an adhesive composition froma soy protein comprising: contacting a soy protein with at least onecompound that includes (i) at least one first functional group selectedfrom phenolic hydroxyl, thiol, amino, or imino, and (ii) at least onesecond functional group; and reacting the soy protein and the compoundunder conditions sufficient for covalently bonding the second functionalgroup of the compound to the soy protein such that the soy proteinstructure is modified to include the first functional group from thecompound.
 22. A method according to claim 21, wherein the secondfunctional group comprises at least one group selected from hydroxyl,carboxyl, or amino.
 23. A method for making a lignocellulosic composite,comprising: applying the adhesive composition of claim 20 to at leastone lignocellulosic substrate; and bonding the adhesive-appliedlignocellulosic substrate to at least one other lignocellulosicsubstrate.
 24. An adhesive composition according to claim 7, wherein thereaction product incorporates about 0.1 weight percent to about 30weight percent of a phenolic hydroxyl compound, an amine compound, animine compound, or a thiol compound.
 25. An adhesive compositionaccording to claim 19, wherein the reaction product incorporates about0.1 weight percent to about 30 weight percent of a phenolic hydroxylcompound, an amine compound, an imine compound, or a thiol compound. 26.A method according to claim 21, further comprising: prior to contactingthe soy protein with the compound, blocking the first functional groupof the compound with a protective group, reacting the protected compoundwith the soy protein resulting in the modified soy protein; and thenremoving the protective group from the modified soy protein.
 27. Anadhesive composition according to claim 19, wherein the first functionalgroup comprises phenolic hydroxyl and the compound is selected fromdopamine, tyramine, DOPA, 2-aminophenol, 3-aminophenol, or4-aminophenol.
 28. An adhesive composition according to claim 19,wherein the first functional group comprises thiol and the compound isselected from cysteamine, cysteine, glutathione, a five-membereddithiocarbonate, γ-thiobutyrolactone, mercaptoacetic acid,2-mercaptoethanol, 3-mercaptopropionic acid, or(3-mercaptopropyl)trimethoxysilane.
 29. An adhesive compositionaccording to claim 19, wherein the first functional group comprisesamino and the compound is selected from an alkyl amine, an unsaturatedhydrocarbon amine, a hydroxy amine, an amidine, an imine, an amino acid,a polyamine, or a polyamide.
 30. An adhesive composition according toclaim 7, wherein the additional functional group comprises an aminogroup.
 31. An adhesive composition according to claim 19, wherein thefirst functional group comprises an amino group.
 32. An adhesivecomposition according to claim 1, wherein the soy protein is provided inthe form of a soy protein product.
 33. An adhesive composition accordingto claim 7, wherein the soy protein is provided in the form of a soyprotein product.
 34. An adhesive composition according to claim 32,wherein the soy protein product is selected from soy flour, soy proteinconcentrate, or soy protein isolate.
 35. An adhesive compositionaccording to claim 33, wherein the soy protein product is selected fromsoy flour, soy protein concentrate, or soy protein isolate.
 36. Anadhesive composition according to claim 34, wherein the soy proteinproduct is soy flour.
 37. An adhesive composition according to claim 35,wherein the soy protein product is soy flour.
 38. A method of making alignocellulosic composite according to claim 8, wherein the soy proteinis provided in the form of a soy protein product.
 39. A method formaking a lignocellulosic composite according to claim 38, wherein thesoy protein product is selected from soy flour, soy protein concentrate,or soy protein isolate.
 40. A method for making a lignocellulosiccomposite according to claim 39, wherein the soy protein product is soyflour.
 41. A method of making an adhesive composition according to claim21, wherein the soy protein is provided in the form of a soy proteinproduct.
 42. A method for making an adhesive composition according toclaim 41, wherein the soy protein product is selected from soy flour,soy protein concentrate, or soy protein isolate.
 43. A method for makingan adhesive composition according to claim 42, wherein the soy proteinproduct is soy flour.